Any feedback?
No. of entries
Information on EC 1.1.5.8 - quinate/shikimate dehydrogenase (quinone)
for references in articles please use BRENDA:EC1.1.5.8
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.5 With a quinone or similar compound as acceptor
1.1.5.8 quinate/shikimate dehydrogenase (quinone)
IUBMB Comments
The enzyme is membrane-bound. Does not use NAD(P)+ as acceptor. Contains pyrroloquinoline-quinone. cf. EC 1.1.1.24, quinate/shikimate dehydrogenase (NAD+), EC 1.1.1.282, quinate/shikimate dehydrogenase [NAD(P)+], and EC 1.1.1.25, shikimate dehydrogenase (NADP+).
The enzyme appears in viruses and cellular organisms
- 1.1.5.8
-
quinoproteins
- gluconobacter
- oxydans
- calcoaceticus
- 3-dehydroquinate
- acinetobacter
- d-glucose
- 3-dehydroshikimate
-
quinohemoprotein
-
methylobacterium
-
holo-forms
showSynonyms
pqq-dependent dehydrogenase, quinoprotein quinate dehydrogenase, nad(p)-independent quinate dehydrogenase, quinate dehydrogenase (quinone), more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dehydrogenase, quinate (pyrroloquinoline-quinone)
-
-
-
-
EC 1.1.99.25
-
-
formerly
-
NAD(P)+-independent quinate dehydrogenase
-
-
-
-
NAD(P)-independent quinate dehydrogenase
PQQ-dependent dehydrogenase
PQQ-QDH
pyrroloquinoline quinone-dependent dehydrogenase
QDH
quiA
quinate dehydrogenase
quinate dehydrogenase (quinone)
-
-
-
-
quinate:pyrroloquinoline-quinone 5-oxidoreductase
-
-
-
-
quinoprotein quinate dehydrogenase
NAD(P)-independent quinate dehydrogenase
-
-
-
-
pyrroloquinoline quinone-dependent dehydrogenase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
quinate + quinone = 3-dehydroquinate + quinol
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
quinate degradation I, shikimate degradation I
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
quinate:quinol 3-oxidoreductase
The enzyme is membrane-bound. Does not use NAD(P)+ as acceptor. Contains pyrroloquinoline-quinone. cf. EC 1.1.1.24, quinate/shikimate dehydrogenase (NAD+), EC 1.1.1.282, quinate/shikimate dehydrogenase [NAD(P)+], and EC 1.1.1.25, shikimate dehydrogenase (NADP+).
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
115299-99-5
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-quinate + tetramethyl-p-phenylenediamine
3-dehydroquinate + reduced tetramethyl-p-phenylenediamine
quinate + 2,6-dichlorophenol indophenol
3-dehydroquinate + reduced 2,6-dichlorophenol indophenol
quinate + 2,6-dichlorophenol-indophenol
3-dehydroquinate + reduced 2,6-dichlorophenol-indophenol
quinate + ?
3-dehydroquinate + ?
-
Substrates: dried cells or dried membrane frations incubated with quinate
Products: -
Products: -
?
shikimate + 2,6-dichlorophenol indophenol
3-dehydroshikimate + reduced 2,6-dichlorophenol indophenol
-
Substrates: reaction rate is 74% of that with quinate, reaction with a combination of phenazine methosulfate and 2,6-dichlorophenol indophenol
Products: -
Products: -
?
shikimate + phenazine methosulfate
3-dehydroshikimate + reduced phenazine methosulfate
-
Substrates: reaction rate is 74% of that with quinate, reaction with a combination of phenazine methosulfate and 2,6-dichlorophenol indophenol
Products: -
Products: -
?
D-quinate + tetramethyl-p-phenylenediamine
3-dehydroquinate + reduced tetramethyl-p-phenylenediamine
-
Substrates: 2,6-dichlorophenolindophenol can also act as electron acceptor
Products: -
Products: -
?
D-quinate + tetramethyl-p-phenylenediamine
3-dehydroquinate + reduced tetramethyl-p-phenylenediamine
-
Substrates: 2,6-dichlorophenolindophenol can also act as electron acceptor
Products: -
Products: -
?
quinate + 2,6-dichlorophenol indophenol
3-dehydroquinate + reduced 2,6-dichlorophenol indophenol
-
Substrates: reaction with a combination of phenazine methosulfate and 2,6-dichlorophenol indophenol
Products: -
Products: -
?
quinate + 2,6-dichlorophenol indophenol
3-dehydroquinate + reduced 2,6-dichlorophenol indophenol
-
Substrates: reaction with a combination of phenazine methosulfate and 2,6-dichlorophenol indophenol
Products: -
Products: -
?
quinate + 2,6-dichlorophenol-indophenol
3-dehydroquinate + reduced 2,6-dichlorophenol-indophenol
Substrates: -
Products: -
Products: -
?
quinate + 2,6-dichlorophenol-indophenol
3-dehydroquinate + reduced 2,6-dichlorophenol-indophenol
Substrates: -
Products: -
Products: -
?
quinate + phenazine methosulfate
3-dehydroquinate + reduced phenazine methosulfate
-
Substrates: reaction with a combination of phenazine methosulfate and 2,6-dichlorophenol indophenol
Products: -
Products: -
?
quinate + phenazine methosulfate
3-dehydroquinate + reduced phenazine methosulfate
-
Substrates: reaction with a combination of phenazine methosulfate and 2,6-dichlorophenol indophenol
Products: -
Products: -
?
quinate + phenazine methosulfate
3-dehydroquinate + reduced phenazine methosulfate
Substrates: -
Products: -
Products: -
?
quinate + phenazine methosulfate
3-dehydroquinate + reduced phenazine methosulfate
Substrates: -
Products: -
Products: -
?
quinate + potassium ferricyanide
3-dehydroquinate + reduced potassium ferricyanide
-
Substrates: -
Products: -
Products: -
?
quinate + potassium ferricyanide
3-dehydroquinate + reduced potassium ferricyanide
-
Substrates: -
Products: -
Products: -
?
quinate + potassium ferricyanide
3-dehydroquinate + reduced potassium ferricyanide
-
Substrates: -
Products: -
Products: -
?
quinate + potassium ferricyanide
3-dehydroquinate + reduced potassium ferricyanide
-
Substrates: -
Products: -
Products: -
?
quinate + potassium ferricyanide
3-dehydroquinate + reduced potassium ferricyanide
-
Substrates: -
Products: -
Products: -
?
quinate + pyrroloquinoline quinone
3-dehydroquinate + pyrroloquinoline quinol
Substrates: -
Products: -
Products: -
r
quinate + pyrroloquinoline quinone
3-dehydroquinate + pyrroloquinoline quinol
Substrates: -
Products: -
Products: -
r
quinate + pyrroloquinoline quinone
3-dehydroquinate + pyrroloquinoline quinol
Substrates: -
Products: -
Products: -
r
quinate + pyrroloquinoline-quinone
3-dehydroquinate + reduced pyrroloquinoline-quinone
-
Substrates: primary enzyme in quinate oxidation
Products: -
Products: -
?
quinate + pyrroloquinoline-quinone
3-dehydroquinate + reduced pyrroloquinoline-quinone
-
Substrates: -
Products: -
Products: -
?
quinate + pyrroloquinoline-quinone
3-dehydroquinate + reduced pyrroloquinoline-quinone
Substrates: QDH shows higher affinity to quinate than to shikimate
Products: -
Products: -
?
quinate + pyrroloquinoline-quinone
3-dehydroquinate + reduced pyrroloquinoline-quinone
Substrates: -
Products: -
Products: -
?
quinate + pyrroloquinoline-quinone
3-dehydroquinate + reduced pyrroloquinoline-quinone
-
Substrates: primary enzyme in quinate oxidation
Products: -
Products: -
?
quinate + pyrroloquinoline-quinone
3-dehydroquinate + reduced pyrroloquinoline-quinone
-
Substrates: -
Products: -
Products: -
?
quinate + pyrroloquinoline-quinone
3-dehydroquinate + reduced pyrroloquinoline-quinone
Substrates: QDH shows higher affinity to quinate than to shikimate
Products: -
Products: -
?
quinate + pyrroloquinoline-quinone
3-dehydroquinate + reduced pyrroloquinoline-quinone
Substrates: -
Products: -
Products: -
?
quinate + pyrroloquinoline-quinone
3-dehydroquinate + reduced pyrroloquinoline-quinone
-
Substrates: primary enzyme in quinate oxidation
Products: -
Products: -
?
quinate + pyrroloquinoline-quinone
3-dehydroquinate + reduced pyrroloquinoline-quinone
-
Substrates: -
Products: -
Products: -
?
quinate + pyrroloquinoline-quinone
3-dehydroquinate + reduced pyrroloquinoline-quinone
-
Substrates: primary enzyme in quinate oxidation
Products: -
Products: -
?
quinate + pyrroloquinoline-quinone
3-dehydroquinate + reduced pyrroloquinoline-quinone
-
Substrates: -
Products: -
Products: -
?
shikimate + potassium ferricyanide
3-dehydroshikimate + reduced potassium ferricyanide
-
Substrates: reaction rate is 74% of that with quinate
Products: -
Products: -
?
shikimate + potassium ferricyanide
3-dehydroshikimate + reduced potassium ferricyanide
-
Substrates: reaction rate is 74% of that with quinate
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is formed in presence or absence of quinate in the culture medium, although stronger induction is usually observed in the presence of quinate. The enzyme directly couples with the respiratory chain of the organisms, yielding bioenergy during substrate oxidation
Products: -
Products: -
?
additional information
?
-
-
Substrates: no oxidation of glucose, 3-dehydroquinate, 3-dehydroshikimate and myo-inositol
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is formed in presence or absence of quinate in the culture medium, although stronger induction is usually observed in the presence of quinate. The enzyme directly couples with the respiratory chain of the organisms, yielding bioenergy during substrate oxidation
Products: -
Products: -
?
additional information
?
-
Substrates: QDH shows higher affinity to quinate, Km 1.0 mM, than to shikimate, Km 9.5 mM
Products: -
Products: -
?
additional information
?
-
Substrates: QDH activity is determined by the quinate-dependent ferricyanide reductase assay, QDH activity is also determined using phenazine methosulfate (PMS) and 2,6-dichlorophenolindophenol (DCIP) and measuring spectrophotometrically at 600 nm
Products: -
Products: -
?
additional information
?
-
Substrates: QDH activity is determined by the quinate-dependent ferricyanide reductase assay, QDH activity is also determined using phenazine methosulfate (PMS) and 2,6-dichlorophenolindophenol (DCIP) and measuring spectrophotometrically at 600 nm
Products: -
Products: -
?
additional information
?
-
-
Substrates: QDH activity is determined by the quinate-dependent ferricyanide reductase assay, QDH activity is also determined using phenazine methosulfate (PMS) and 2,6-dichlorophenolindophenol (DCIP) and measuring spectrophotometrically at 600 nm
Products: -
Products: -
?
additional information
?
-
Substrates: QDH shows higher affinity to quinate, Km 1.0 mM, than to shikimate, Km 9.5 mM
Products: -
Products: -
?
additional information
?
-
Substrates: QDH activity is determined by the quinate-dependent ferricyanide reductase assay, QDH activity is also determined using phenazine methosulfate (PMS) and 2,6-dichlorophenolindophenol (DCIP) and measuring spectrophotometrically at 600 nm
Products: -
Products: -
?
additional information
?
-
Substrates: QDH activity is determined by the quinate-dependent ferricyanide reductase assay, QDH activity is also determined using phenazine methosulfate (PMS) and 2,6-dichlorophenolindophenol (DCIP) and measuring spectrophotometrically at 600 nm
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
quinate + pyrroloquinoline quinone
3-dehydroquinate + pyrroloquinoline quinol
Substrates: -
Products: -
Products: -
r
quinate + pyrroloquinoline quinone
3-dehydroquinate + pyrroloquinoline quinol
Substrates: -
Products: -
Products: -
r
quinate + pyrroloquinoline quinone
3-dehydroquinate + pyrroloquinoline quinol
Substrates: -
Products: -
Products: -
r
quinate + pyrroloquinoline-quinone
3-dehydroquinate + reduced pyrroloquinoline-quinone
-
Substrates: primary enzyme in quinate oxidation
Products: -
Products: -
?
quinate + pyrroloquinoline-quinone
3-dehydroquinate + reduced pyrroloquinoline-quinone
Substrates: QDH shows higher affinity to quinate than to shikimate
Products: -
Products: -
?
quinate + pyrroloquinoline-quinone
3-dehydroquinate + reduced pyrroloquinoline-quinone
-
Substrates: primary enzyme in quinate oxidation
Products: -
Products: -
?
quinate + pyrroloquinoline-quinone
3-dehydroquinate + reduced pyrroloquinoline-quinone
Substrates: QDH shows higher affinity to quinate than to shikimate
Products: -
Products: -
?
quinate + pyrroloquinoline-quinone
3-dehydroquinate + reduced pyrroloquinoline-quinone
-
Substrates: primary enzyme in quinate oxidation
Products: -
Products: -
?
quinate + pyrroloquinoline-quinone
3-dehydroquinate + reduced pyrroloquinoline-quinone
-
Substrates: primary enzyme in quinate oxidation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is formed in presence or absence of quinate in the culture medium, although stronger induction is usually observed in the presence of quinate. The enzyme directly couples with the respiratory chain of the organisms, yielding bioenergy during substrate oxidation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is formed in presence or absence of quinate in the culture medium, although stronger induction is usually observed in the presence of quinate. The enzyme directly couples with the respiratory chain of the organisms, yielding bioenergy during substrate oxidation
Products: -
Products: -
?
additional information
?
-
Substrates: QDH shows higher affinity to quinate, Km 1.0 mM, than to shikimate, Km 9.5 mM
Products: -
Products: -
?
additional information
?
-
Substrates: QDH shows higher affinity to quinate, Km 1.0 mM, than to shikimate, Km 9.5 mM
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyrroloquinoline quinone
PQQ-dependent dehydrogenase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
quinate dehydrogenase holoenzyme and quinate dehydrogenase apoenzyme after recombination with pyrroloquinoline quinone is not affected by EDTA
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.26
shikimate
-
pH 6.5, 25°C, with potassium ferricyanide or a combination of phenazine methosulfate and 2,6-dichlorophenol indophenol as electron acceptor
0.2
quinate
-
pH 6.5, 25°C,with potassium ferricyanide or a combination of phenazine methosulfate and 2,6-dichlorophenol indophenol as electron acceptor
1
quinate
pH 8.0, temperature not specified in the publication, recombinant enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 6
-
quinate oxidation with potassium ferricyanide or a combination of phenazine methosulfate and 2,6-dichlorophenol indophenol
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
and strains SA4, SA5, SA6, SA7, SA8, SA9, SA10, SA11, SA12 and SA13, isolated in Thailand
-
-
brenda
and strains SA4, SA5, SA6, SA7, SA8, SA9, SA10, SA11, SA12 and SA13, isolated in Thailand
-
-
brenda
no activity in Gluconobacter frateurii
IFO 3251, IFO 3264, CHM 16, CHM 54 and IFO 3286
-
-
brenda
no activity in Gluconobacter oxydans
IFO 3130, IFO 3172, IFO 3290, IFO 3289, IFO 12528, var. alphaIFO3254, car. alphaIFO 3255, var. alphaIFO 3256, var. alphaIFO 3257 and car. alphaIFO3258
-
-
brenda
IFO 3292 and IFO 3244. No activity in IFP3990, IFO3189, IFO 3287, ATCC 621 and IFO 14819
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
evolution
phylogenetic distribution of QDH with in the membrane-bound, PQQ-dependent proteins of the publicly available Gluconobacter genomes, overview
evolution
phylogenetic distribution of QDH with in the membrane-bound, PQQ-dependent proteins of the publicly available Gluconobacter genomes, overview. The genetic sequence of the QDH of NBRC3292 is identical to that of NBRC3244, while the QDH of NBRC3293 is different in 7 amino acids from that of NBRC3244
evolution
-
phylogenetic distribution of QDH with in the membrane-bound, PQQ-dependent proteins of the publicly available Gluconobacter genomes, overview. The genetic sequence of the QDH of NBRC3292 is identical to that of NBRC3244, while the QDH of NBRC3293 is different in 7 amino acids from that of NBRC3244
-
evolution
-
phylogenetic distribution of QDH with in the membrane-bound, PQQ-dependent proteins of the publicly available Gluconobacter genomes, overview
-
physiological function
Gluconobacter oxydans produces 3-dehydroquinate by oxidation of quinate through a reaction catalyzed by the quinate dehydrogenase (QDH), membrane-bound, pyrroloquinoline quinone (PQQ)-dependent dehydrogenase
physiological function
-
Gluconobacter oxydans produces 3-dehydroquinate by oxidation of quinate through a reaction catalyzed by the quinate dehydrogenase (QDH), membrane-bound, pyrroloquinoline quinone (PQQ)-dependent dehydrogenase
-
physiological function
-
Gluconobacter oxydans produces 3-dehydroquinate by oxidation of quinate through a reaction catalyzed by the quinate dehydrogenase (QDH), membrane-bound, pyrroloquinoline quinone (PQQ)-dependent dehydrogenase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). QUIA_ACIAD
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
809
5
88196
Swiss-Prot
other Location (Reliability: 1)
QUIA_XANCJ
790
4
82897
Swiss-Prot
other Location (Reliability: 2)
A0A2Z5U248_GLUOY
822
0
88533
TrEMBL
other Location (Reliability: 2)
B9TTF1_GLUOY
824
0
88962
TrEMBL
Secretory Pathway (Reliability: 5)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
x * 88600, about, sequence calculation, x * 100000, recombinant enzyme, SDS-PAGE
?
-
x * 88600, about, sequence calculation, x * 100000, recombinant enzyme, SDS-PAGE
-
additional information
-
on addition of pyrroloquinoline quinone the purified apoenzyme is conveted from a dimer to a monomer
additional information
-
on addition of pyrroloquinoline quinone the purified apoenzyme is conveted from a dimer to a monomer
-
additional information
prediction of secondary structure of the mRNA
additional information
prediction of secondary structure of the mRNA
additional information
-
prediction of secondary structure of the mRNA
-
additional information
-
prediction of secondary structure of the mRNA
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from cell membranes by dilution in 10 mM Tris-HCl, pH 7.5, 1 mM CaCl2, and 1% w/v DDM at the final protein concentration of 10 mg/ml followed by incubation for 30 min at 4°C with gentle mixing and ultracentrifugation at 100000 × g for 30 min at 4°C. The resultant supernatant containing the solubilized membranes is resuspended with the same volume of 10 mM Tris-HCl, pH 7.5, and 1 mM CaCl2. The enzyme is solublized from membranes and purified by anion exchange chromatography, dialysis, and hydroxyapatite chromatography
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene qdh, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, expression in pyrroloquinoline quinone synthesizing Pseudomonas putida strain HK5
gene quiA, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree, heterologous expression of QDH in Gluconobacter frateurii, improvement of the heterologous expression of QDH in Gluconobacter strains using a broad-host-range plasmid, best with a long 5'-UTR. Gluconobacter oxydans strain NBRC12528 DELTAadhA::KmR is transformed by triparental mating using Escherichia coli HB101 harboring pRK2013 as the helper strain, Gluconobacter frateurii strain SEI46 (DELTAadhAB) is transformed with the same plasmids by electroporation
gene quiA, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree, QDH translates from the second TTG codon: Met-His-Ser-Ile-Asp, heterologous expression of QDH in Gluconobacter frateurii, improvement of the heterologous expression of QDH in Gluconobacter strains using a broad-host-range plasmid, best with a long 5'-UTR. Gluconobacter oxydans strain NBRC12528 DELTAadhA::KmR is transformed by triparental mating using Escherichia coli HB101 harboring pRK2013 as the helper strain, Gluconobacter frateurii strain SEI46 (DELTAadhAB) is transformed with the same plasmids by electroporation. Change of the initiation codon to ATG does not improve QDH activity but results in expression levels similar to those achieved with the wild-type plasmid
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Van Kleef, M.A.G.; Duine, J.A.
Bacterial NAD(P)-independent quinate dehydrogenase is a quinoprotein
Arch. Microbiol.
150
32-36
1988
Acinetobacter calcoaceticus, Acinetobacter calcoaceticus LMD 79.41
brenda
Adachi, O.; Yoshihara, N.; Tanasupawat, S.; Toyama, H.; Matsushita, K.
Purification and characterization of membrane-bound quinoprotein quinate dehydrogenase
Biosci. Biotechnol. Biochem.
67
2115-2123
2003
Acinetobacter calcoaceticus, no activity in Gluconobacter gluconicus, no activity in Gluconobacter industrius, no activity in Gluconobacter sphaericus, no activity in Gluconobacter oxydans, Gluconobacter oxydans, Acinetobacter sp., no activity in Gluconobacter asaii, no activity in Gluconobacter albidus, no activity in Gluconobacter cerinus, no activity in Gluconobacter dioxyacetonicus, no activity in Gluconobacter frateurii, Acinetobacter sp. SA1, Acinetobacter calcoaceticus AC3
brenda
Adachi, O.; Tanasupawat, S.; Yoshihara, N.; Toyama, H.; Matsushita, K.
3-Dehydroquinate production by oxidative fermentation and further conversion of 3-dehydroquinate to the intermediates in the shikimate pathway
Biosci. Biotechnol. Biochem.
67
2124-2131
2003
Gluconobacter sp., Gluconobacter oxydans, Gluconobacter sp. IFO 3244, Gluconobacter oxydans IFO 3294
brenda
Adachi, O.; Ano, Y.; Toyama, H.; Matsushita, K.
High shikimate production from quinate with two enzymatic systems of acetic acid bacteria
Biosci. Biotechnol. Biochem.
70
2579-2582
2006
Gluconobacter oxydans
brenda
Vangnai, A.S.; Promden, W.; De-Eknamkul, W.; Matsushita, K.; Toyama, H.
Molecular characterization and heterologous expression of quinate dehydrogenase gene from Gluconobacter oxydans IFO3244
Biochemistry (Moscow)
75
452-459
2010
Gluconobacter oxydans (B9TTF1), Gluconobacter oxydans IFO3244 (B9TTF1)
brenda
Yakushi, T.; Komatsu, K.; Matsutani, M.; Kataoka, N.; Vangnai, A.S.; Toyama, H.; Adachi, O.; Matsushita, K.
Improved heterologous expression of the membrane-bound quinoprotein quinate dehydrogenase from Gluconobacter oxydans
Protein Expr. Purif.
145
100-107
2018
Gluconobacter oxydans (A0A2Z5U248), Gluconobacter oxydans (A0A2Z5U421), Gluconobacter oxydans, Gluconobacter oxydans NBRC3244 (A0A2Z5U421), Gluconobacter oxydans NBRC3293 (A0A2Z5U248)
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.5.8)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
